Q2UFN3 (NCB5R_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-cytochrome b5 reductase 1
EC=1.6.2.2

Alternative name(s):
Microsomal cytochrome b reductase

Gene names

Name:	cbr1
ORF Names:	AO090026000138

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Electron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Mitochondrion outer membrane; Single-pass membrane protein By similarity.
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.
Sequence caution	The sequence BAE59632.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	NADH-cytochrome b5 reductase 1		PRO_0000330146
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Domain	43 – 148	106	FAD-binding FR-type
	Nucleotide binding	128 – 143	16	FAD By similarity
	Nucleotide binding	154 – 191	38	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2UFN3 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 15E3E5EA7D7E8A3D	FASTA	292	31,925
	10 20 30 40 50 60 MSAFASENLT SALLVVGTAI FAVLVGAKFL GGSGKPRKVL NPTEFQNFVL KEKNEISHNV 70 80 90 100 110 120 AIYRFALPRP TDILGLPIGQ HISLAATIEG QPKEVVRSYT PISSDNEAGY FDLLVKAYPQ 130 140 150 160 170 180 GNISKYLTTL KIGDNMKVRG PKGAMVYTPN MCRHIGMIAG GTGITPMLQI IKAIIRNRPR 190 200 210 220 230 240 NGGNDTTQVD LIFANVNPED ILLKEELEQL VKEDDGFRVY YVLNNPPEGW TGGVGFVTPD 250 260 270 280 290 MIKERLPAPA QDIKIMLCGP PPMISAMKKA TESLGYTKAR PVSKLEDQVF CF

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007159 Genomic DNA. Translation: BAE59632.1. Sequence problems.
RefSeq	XP_001821634.2. XM_001821582.2.
3D structure databases
ProteinModelPortal	Q2UFN3.
SMR	Q2UFN3. Positions 35-279.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5993662.
GenomeReviews	Gene locus cbr1 in contig AP007159_GR.
KEGG	aor:AOR_1_264014.
Phylogenomic databases
GeneTree	EFGT00050000001026.
OrthoDB	EOG4FFH9R.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
KO	K00326.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCB5R_ASPOR

Accession

Primary (citable) accession number: Q2UFN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	January 25, 2012
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program